Epigenetic regulation of glycosylation is the quantum mechanics of biology

Most proteins are glycosylated, with glycans being integral structural and functional components of a glycoprotein. In contrast to polypeptides, which are fully encoded by the corresponding gene, glycans result from a dynamic interaction between the environment and a network of hundreds of genes. Re...

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Published inBiochimica et biophysica acta Vol. 1840; no. 1; pp. 65 - 70
Main Authors Lauc, Gordan, Vojta, Aleksandar, Zoldoš, Vlatka
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.01.2014
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Summary:Most proteins are glycosylated, with glycans being integral structural and functional components of a glycoprotein. In contrast to polypeptides, which are fully encoded by the corresponding gene, glycans result from a dynamic interaction between the environment and a network of hundreds of genes. Recent developments in glycomics, genomics and epigenomics are discussed in the context of an evolutionary advantage for higher eukaryotes over microorganisms, conferred by the complexity and adaptability which glycosylation adds to their proteome. Inter-individual variation of glycome composition in human population is large; glycome composition is affected by both genes and environment; epigenetic regulation of “glyco-genes” has been demonstrated; and several mechanisms for transgenerational inheritance of epigenetic marks have been documented. Epigenetic recording of acquired characteristics and their transgenerational inheritance could be important mechanisms used by higher organisms to compete or collaborate with microorganisms. •The majority of proteins are glycosylated.•Glycan parts of proteins perform numerous structural and functional roles•There are no genetic templates for glycans, instead glycans are defined by dynamic interaction between genes and environment.•Epigenetic changes enable adaptation to variations in environment.•Epigenetic regulation of glyco—genes is a powerful evolutionary tool.
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ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/j.bbagen.2013.08.017